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β-Hairpin Folding Mechanism of a Nine-Residue Peptide Revealed from Molecular Dynamics Simulations in Explicit Water

The β-hairpin fold mechanism of a nine-residue peptide, which is modified from the β-hairpin of α-amylase inhibitor tendamistat (residues 15–23), is studied through direct folding simulations in explicit water at native folding conditions. Three 300-nanosecond self-guided molecular dynamics (SGMD) s...

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Bibliografski detalji
Glavni autori: Wu, Xiongwu, Brooks, Bernard R.
Format: Artigo
Jezik:Inglês
Izdano: Biophysical Society 2004
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1304050/
https://ncbi.nlm.nih.gov/pubmed/15041639
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